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OJBTM
Online Journal of Bioinformatics©
Volume 22 (3): 165-174,
2021.
In-silico polymorphism
and structure of human retinal-aldehyde-binding protein 1.
Muhammad Ilyas and Khalid Masood
National Center of Excellence in Molecular
Biology, University of the Punjab, Lahore, Bioinformatics Laboratory, National
Center of Excellence in Molecular Biology, University of the Punjab Lahore
India
ABSTRACT
Ilyas M, Masood K., In-silico polymorphism and structure of
human retinal-aldehyde-binding protein 1,, Onl J Bioinform., 22 (3): 175-188, 2021. Cellular
retinaldehyde binding protein (CRALBP), a 36-kD
water-soluble protein occurs in retina and pineal gland with 11-cis- retinaldehyde or 11-cis-retinal ligands. Human retinal-aldehyde-binding
protein 1 (RLBP1) gene was searched for single nucleotide
polymorphisms (SNP) revealing 116 of 3 non-synonymous (nsSNP)
and 1 in synonymous regions. Non-coding areas comprised 7 SNPs in UTR and 98 in
introns. The 3 nsSNPs transcription factor binding
sites included G/A SNP, arginine to glutamine substitution, C/T SNP arginine to
tryptophan and C/G/A SNP histidine to glutamine. The model revealed SNP
position 151, 234 and 269 mutated for changes in protein structure. Model hydrogen
bonding, ion pairs and accessibility are described. We report In silico association of RLBP1 SNPs with night vision
blindness, Bothnia retinal and Newfoundland rod-cone dystrophies and Fundus Albipunctatus.
Mutations in the domain could decrease the interactions between the residues
causing unstability.
Key words: RLBP1, nsSNPs, Homology modeling,
11-cis- retinaldehyde.
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